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      • Beneficial Effects of Resveratrol on Bovine Oocyte Maturation and Subsequent Embryonic Development After IVF

        Feng Wang,XiuZhi Tian,Lu Zhang,ChangJiu He,PengYun Ji,Yu Li,DunXian Tan,GuoShi Liu 한국동물생명공학회(구 한국동물번식학회) 2014 한국동물번식학회 한중일 심포지엄 Vol.2014 No.1

        Objective: To analyze the potential beneficial effects and mechanisms of action of resveratrol on the maturation of bovine oocytes that were incubated in different concentrations of resveratrol (0.1, 1.0 or 10μM) as germinal vesicle (GV) oocytes. Design: In vitro prospective study. Setting: University research laboratory Patient(s): Animal models for human studies. Intervention(s): In vitro culture in the presence of various concentrations of the antioxidant resveratrol. Main Outcome Measures: The parameters of hormone levels, oocyte nuclear maturation, cumulus expansion, levels of intracellular glutathione and reactive oxygen species, embryonic cleavage, blastocyst formation, gene expression associated with mature bovine oocytes and cumulus cells and the level of sirtuin 1 gene expression were detected. Results: Resveratrol significantly increased progesterone secretion and decreased estradiol- 17β secretion by cumulus cells. The elevated levels of progesterone activated the Mos/MEK/p42 MAPK cascade in the oocytes. At a concentration of 1.0 μM, resveratrol significantly improved cumulus expansion, polar body formation, the (hatched)blastocyst rate and the mean number of cells/blastocyst. Meanwhile, resveratrol significantly reduced the level of ROS, increased the level of GSH. For the first time, the expression of the sirtuin 1 gene was identified in granulosa cells, cumulus cells, oocytes and blastocysts. Further studies revealed that resveratrol promoted sirtuin 1 gene expression.Conclusion(s): Resveratrol promoted bovine oocyte maturation and subsequent post- IVF embryonic development by inducing progesterone secretion and antioxidant effect, probably in a manner dependent on Sirtuin 1.

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        Hydrophilic Finishing of PET Fabrics by Applying Chitosan and the Periodate Oxidized β-cyclodextrin for Wash Resistance Improvement

        Chaoqian Lou,Yuanyuan Yin,Xiuzhi Tian,Haibo Deng,Yingxia Wang,Xue Jiang 한국섬유공학회 2020 Fibers and polymers Vol.21 No.1

        β-cyclodextrin (β-CD) was oxidized by sodium periodate to yield a mixture of dialdehyde oligosaccharides. Theperiodate-oxidized β-CD (O-β-CD) together with chitosan (CTS) was firstly used to finish poly(ethylene terephthalate)(PET) fabrics by immersion-padding method, in which O-β-CD acted as a hydrophilic finishing agent plus a cross-linker. Theprocesses including the periodate oxidization of β-CD and the CTS/O-β-CD hydrophilic finishing of PET fabrics were ecofriendly. The results from the hydroxylamine hydrochloride titration showed that the aldehyde content in O-β-CD was3.0 mmol/g. With increasing the CTS/O-β-CD mass ratio, the finished fabric had better hydrophilic properties. When theCTS/O-β-CD mass ratio was 1:1, the moisture regain and water drops wetting time of the finished fabric reached 1.85 % and5.06 s, respectively. They became 1.50 % and 5.70 s, respectively after 25 times of laundering cycle. The occurrence of crosslinkingbetween O-β-CD and CTS was confirmed by the gel test and FT-IR characterization. The cross-linking networkdeposited on the fiber surface brought on excellent wash resistance of the CTS/O-β-CD finished PET fabrics.

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        Modification of Wool via Grafting β-cyclodextrin Oxidized by Sodium Periodate

        Chaoqian Lou,Yuanyuan Yin,Xiuzhi Tian,Haibo Deng,Yingxia Wang,Xue Jiang 한국섬유공학회 2020 Fibers and polymers Vol.21 No.8

        The modification of wool fabrics is significant in preparation of functional textiles. Sodium periodate oxidized β-cyclodextrin was grafted onto wool fabric through Schiff base reaction to obtain fabric with controlled release property. β-cyclodextrin was oxidized to aldehyde-β-cyclodextrin, and the results show that the inclusion constant and aldehyde contentof aldehyde-β-cyclodextrin are varied with the reaction parameters such as molar ratio of reaction agents and the reactiontemperature. The degree of oxidation was confirmed by ion chromatography. The drug loading test shows that the oxidizedcyclodextrin still had inclusion ability towards phenolphthalein, while the inclusion constant was only 50 % of the original β-CD. The ATR-FTIR spectra proved the occurrence of grafting reaction between the aldehyde groups of aldehyde-β-cyclodextrin and the amino groups on wool fiber. The aldehyde-β-cyclodextrin grafted wool fabric show great washingdurability even after 5 washing cycles. Compared with the aldehyde-β-cyclodextrin power, the inclusion ability of aldehyde-β-cyclodextrin fixed on the wool fiber decreased by 60 %.

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        Death-associated protein kinase 1 phosphorylates MDM2 and inhibits its protein stability and function

        Mi Zhang,Xindong Shui,Xiaoqing Zheng,Jong Eun Lee,Yingxue Mei,Ruomeng Li,Yuan Tian,Xiuzhi Zheng,Quling Wang,Long Wang,Dongmei Chen,Tao Zhang,Byeong Mo Kim,Jungho Kim,Tae Ho Lee 대한약학회 2023 Archives of Pharmacal Research Vol.46 No.11

        Breast cancer is one of the major malignancies in women, and most related deaths are due to recurrence, drug resistance, and metastasis. The expression of the mouse double minute 2 (MDM2) oncogene is upregulated in breast cancer; however, its regulatory mechanism has yet to be fully elucidated. Herein, we identified the tumor suppressor death-associated protein kinase 1 (DAPK1) as a novel MDM2 regulator by unbiased peptide library screening. DAPK1 is directly bound to MDM2 and phosphorylates it at Thr419. DAPK1-mediated MDM2 phosphorylation promoted its protein degradation via the ubiquitin–proteasome pathway, resulting in upregulated p53 expression. DAPK1 overexpression, but not its kinase activity-deficient form, decreased colony formation and increased doxorubicin-induced cell death; however, DAPK1 knockdown produced the opposite effects in human breast cancer cells. In a xenograft tumorigenesis assay, DAPK1 overexpression significantly reduced tumor formation, whereas inhibition of DAPK1 kinase activity reduced its antitumorigenic effect. Finally, DAPK1 expression was negatively correlated with MDM2 levels in human breast cancer tissues. Thus, these results suggest that DAPK1-mediated MDM2 phosphorylation and its protein degradation may contribute to its antitumorigenic function in breast cancer.

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